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Quantitative proteomic and phosphoproteomic analyses reveal salt tolerance mechanisms of the halophyte Hordeum brevisubulatum

文献类型： 外文期刊

作者： Feng, Hao 1 ; Zhao, Jielong 2 ; Xiao, Fang 1 ; Wang, Shuyue 4 ; Jiang, Ying 1 ; Lu, Yuncai 2 ; Li, Ruifen 1 ;

作者机构： 1.Beijing Acad Agr & Forestry Sci, Inst Biotechnol, Beijing Key Lab Agr Genet Resources & Biotechnol, Beijing Key Lab Crop Mol Design & Intelligent Bree, Beijing, Peoples R China

2.Heilongjiang Univ, Coll Adv Agr & Ecol Environm, Harbin 150080, Peoples R China

3.Beijing Univ Agr, Coll Plant Sci & Technol, Beijing, Peoples R China

4.JiNing Normal Coll, Jining, Inner Mongolia, Peoples R China

关键词： Salt stress; Protein abundance; Protein phosphorylation; Dehydrin; Crop wild relative

期刊名称：PLANT PHYSIOLOGY AND BIOCHEMISTRY （ 影响因子：5.7； 五年影响因子：6.4 ）

ISSN： 0981-9428

年卷期： 2025 年 228 卷

页码：

收录情况： SCI

摘要： Soil salinization increasingly threatens global agriculture. Plants employ adaptive mechanisms, with protein phosphorylation being crucial for rapid stress responses. Halophytes like Hordeum brevisubulatum, a wild relative of barley and wheat, exhibit remarkable salt tolerance, but the underlying molecular mechanisms, particularly the role of dynamic phosphorylation, are not fully understood. Comparative physiological analyses confirmed the superior salt tolerance of H. brevisubulatum compared to cultivated barley. Time-resolved quantitative proteomics and phosphoproteomics were employed to capture the dynamic molecular landscape of H. brevisubulatum under salt stress. Proteomics analysis revealed progressive changes, with upregulation of stress-related proteins and downregulation of biosynthetic pathways, including a notable switch in branched-chain amino acid metabolism. Phosphoproteomics identified hundreds of differentially phosphorylated sites with distinct temporal dynamics, implicating phosphorylation in regulating key proteins involved in signaling, ion and water transport, and ROS homeostasis. Phosphorylation motif analysis revealed conserved and potentially adaptive phosphorylation patterns, such as that of aquaporin PIP2;5 at S289, which modulates its water transport activity. Furthermore, we functionally validated that the dehydrin HbDHN3 enhances salt tolerance, and that its phosphorylation, potentially mediated by HbCK2, significantly boosts this protective function in transgenic Arabidopsis. This study presents an integrated proteomic and phosphoproteomic investigation into the salt adaptation mechanisms of H. brevisubulatum. Our findings underscore the sophisticated coordination between changes in protein levels and dynamic phosphorylation events across signaling, transport, ROS management, and metabolism. The functional validation of candidate proteins confirms the power of our integrated approach to identify critical effectors of stress tolerance, providing a robust dataset and valuable insights for crop improvement against salinity.

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